Molecular Biomimetics: Genetic Synthesis, Assembly, and Formation of Materials Using Peptides

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tide fabrication and assembly processes take place under ambient and environ- mentally friendly conditions.1–11 Gaining the ability to closely manipulate the Molecular behavior of peptides to fully control materials formation would be a giant leap toward realizing nanometer-scale Biomimetics: building blocks that tailor electronic, optical, mechanical, or magnetic materials properties.25 Molecular biology and genetics approaches could modify the polypep- Genetic Synthesis, tides and their molecular-recognition characteristics,11–15 and traditional and state-of-the-art engineering approaches16 could create inorganic or synthetic struc- Assembly, and tures such as nanoparticles,17–20 quantum dots,20 molecular wires21 or nanowires,22 or synthetic molecular systems23 (e.g., organic semiconductors).24 Formation of Proteins are long peptide chains that have diverse properties deriving from the specific amino-acid sequences and the physical chain architectures. The wide Materials Using degree of conformational freedom allows proteins to readily adapt to their environ- ment, and the variability in the genetic Peptides sequence and the conformational freedom gives a protein its crucial functionalities.26,27 Proteins inherently have the Candan Tamerler and Mehmet Sarikaya, largest information content among all the biological macromolecules (including Guest Editors DNA, polysaccharides, and lipids). There- fore, proteins are the “machinery” that accomplish a myriad of functions through Abstract their specific recognition and interactions In nature, the molecular-recognition ability of peptides and, consequently, their with biomolecules and that are vital to the functions are evolved through successive cycles of mutation and selection. Using life of single-celled and multicellular biology as a guide, it is now possible to select, tailor, and control peptide–solid organisms.26,27 interactions and exploit them in novel ways. Combinatorial mutagenesis provides a For example, in the biological hard tis- 28 protocol to genetically select short peptides with specific affinity to the surfaces of a sues (Figure 1) in the skeletons of many 29–31 32 variety of materials including metals, ceramics, and semiconductors. In the articles of organisms, in bacterial thin films or 33,34 28 35 this issue, we describe molecular characterization of inorganic-binding peptides; explain nanoparticles (Figure 1a), in cuticles, 29,36 37 their further tailoring using post-selection genetic engineering and bioinformatics; and spines, and spicules (Figure 1b), or 38–40 41 finally demonstrate their utility as molecular synthesizers, erectors, and assemblers. in shells (Figure 1c), biomolecule– The peptides become fundamental building blocks of functional materials, each material interaction is accomplished via 42,43 uniquely designed for an application in areas ranging from practical engineering molecular specificity. This leads to the formation of controlled architectures and to medicine. functions at all scales of dimensional hier- archy.29,44 A more detailed example is mammalian tooth organ.45 In this case, of the six tissues present, four (cementum, Introduction dentin, enamel, and bone) contain a min- Molecular biomimetics is an emerging of designer proteins (such as enzymes) that eral—hydroxyapatite (HA)—as the same key field in science and technology.1 have useful characteristics. The central inorganic component (Figure 1d).46 Through the use of recombinant DNA premise of this interdisciplinary field is Although the HA particles are the major methods, combinatorial approaches have that genetically engineered peptides for component in all hard tissues in tooth,46 as been developed to select and tailor pep- inorganics (GEPIs)1 can be utilized as well as in skeletal bone,47 neither the struc- tides with properties not present in nature. molecular erector sets.2–6 With molecular ture of the individual HA crystallites nor A peptide is two or more amino acids biomimetics methods, peptides may direct their crystallography or overall organiza- linked in a chain. Peptides have desirable synthesis, fabrication, assembly, and archi- tion are the same in any two of these com- inorganic-binding and assembly character- tecture of hybrid materials, creating mate- plex composites, which are particle-filled istics and can be used as molecular build- rials with programmed composition, polymeric nanocomposites.48 Among these ing blocks in practical applications.2–6 The phase, and topology. Such materials could tissues, the enamel of the tooth’s crown peptides work either in isolation or when have designed and controlled functions at provides the hardest material for the body. inserted within the structural framework the molecular or nanometer scale. The pep- Enamel contains almost 99% ceramic

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trolled molecular-scale organization. Such Magnetotactic Nanomagnetics Hierarchical Structure of molecular-scale control could lead to Bacteria Mammalian Tooth designed functionality with practical implications in a wide range of interdisci- 100 µm plinary fields.1,28,53–55 Examples include E immobilizing nanoinorganic particles on D 1 cm Bulk molecular or solid substrates, developing peptide- based molecular probes, and surface engineering of inorganics. If these P Macro developments are accomplished, some of current limitations in molecular technol- 500nm PDL a 50 nm ogy and nanotechnology could be over- C come by bridging dissimilar materials Optical Sponge components with high complexity and assembling molecular and inorganic Spicules nano- components in hybrid systems with B B specific size, shape, and spatial organiza- 10 mm tion.56–60 The biomimetic materials field m 1 mm 200 m Nano 150 nm is now mature enough to address funda- b mental issues at the confluence of materi- Nanomechanics als and biology and to provide practical solutions in engineering and medical fields. This article highlights the selection m 5 m of peptides that bind to solid substrates, the degree of binding, and the use of pep- Micro 1 µm tides as building blocks, and provides a c d guide for future directions.

Figure 1. Examples of highly evolved hard tissues from various organisms, controlled by Selection of Inorganic-Binding proteins with engineering functions. (a) Magnetite particles in a magnetotactic bacterium, Peptides Using Combinatorial Aquaspirillum magnetotacticum, form a magnetic compass (from Reference 28). Mutagenesis (b) Spicules of the deep-sea sponge Rosella have optical characteristics comparable to For the last two decades, combinatorial synthetic optical fibers (from Reference 37); a light optical image shows a star-shaped lens biological-display technologies have been at the tip of a spicule, and a secondary electron image shows the fractured surface of a developed for a myriad of biological spicule revealing layered microstructure. (c) The mother-of-pearl of red abalone shell and biotechnological applications. A − (Haliotis Rufescens) has a highly desirable toughness strength combination arising from its biological-display technology is a bacteria unique brick-and-mortar nano-/micro-architecture consisting of CaCO3 platelets in the aragonite phase layered with protein/polysaccharide (from Reference 40). (d) Hierarchical or phage (a virus that infects a bacteria) architecture of the mammalian enamel at the crown of the tooth (from Reference 46). engineered to exhibit a peptide sequence Enamel (E) forms an integrated structure with the dentin (D) underneath at the bulk scale. on the membrane protein of the bacteria The enamel has an architecture of woven enamel rods (3 µm diameter) at the micrometer or on the coat protein of the phage. scale, each rod containing thousands of long HA crystallites (10s of nm thick and several Applications range from the examination mm long), all spatially and crystallographically well-organized on the nanometer scale. of receptor–antibody interactions and the study of protein–ligand interactions to the isolation and directed evolution of material and is a protective cover to the well-integrated transition called the enzymes and proteins for enhanced catal- dental tissues of all mammalians.49 dentin-enamel junction.46,51 Despite the ysis or altered binding characteristics.61–65 HA has a different architecture in each enormous work invested in isolating Among the display technologies, the of the hierarchical scales. The specific many of the proteins and identifying their in vivo selection of peptides using cell- structures are controlled by numerous function in controlling mineralization and surface display (CSD) and phage display proteins such as amelogenin and tuftelin. buildup of tissues and despite the knowl- (PD) has been used most frequently Each of these proteins plays a critical role edge that protein absence leads to genetic (Figure 2).9 CSD is a technology whereby in controlling various structural features diseases such as amelogenin imperfecta,52 a peptides appear on the flagella of a bacte- in the complex, highly evolved, and func- thorough understanding of spatial and rial cell membrane. PD is a technology tional enamel tissue.49,50 During the pro- temporal distributions of the proteins and whereby peptides appear on the coat pro- duction of the material, the proteins assist their isolated or collective roles in forming tein of a phage. These approaches have or direct the processes of nucleation, the complex enamel structure has so far been adapted to select peptides that bind growth, morphogenesis, and ordering been elusive.49,50 to solid inorganic materials.1,3–9,55–59,66 that lead to enamel rods containing thou- Similar to natural, biological proteins The articles by Evans et al. and Tomczak sands of HA nanoparticles—all organized that evolve into highly specialized mole- et al. in this issue explain combinatorial with well-defined crystallography—and cules with specific functions, engineered mutagenesis, the method of creating a to the final woven architecture of the rods. peptides (and designer proteins) in molec- large set of phage or bacteria—each The latter area is where the overall tissue ular biomimetics could also be of great displaying a peptide with a random is integrated with the underlying tougher, utility. By design, the peptides could sequence—and the biopanning process, bone-like dentin structure—providing a synthesize, assemble, and form solid- the method that culls the set to obtain only mechanically and structurally smooth and containing materials that have con - the peptide sequences that selectively bind

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to a desired substrate or that have particu- a lar binding properties. Figure 2 provides Generation of Libraries: an overview of combinatorial mutagenesis and biopanning, and the article by Sano randomized et al. in this issue provides a specific exam- oligonucleotides (RO) ple of binding to nanoparticles. Inorganic materials are very different Insertion of RO into genes encoded on phage genomes or bacterial plasmids substrates than proteinaceous or gen - eral biomolecular ligands.61–65 Therefore, Phage Bacterial Cell adapting biological display technologies for the realm of materials science would require a new set of conditions and proto- cols, though this has not been widely discussed in the literature so far.55 Inorganic compounds come in a variety of forms, Display of random amino-acid sequences from morphologically uncharacterized on the coat protein of a phage or flagella powders of various particle sizes to single crystals with crystallographically defined flat surfaces. The chemical or physical Cleaning & Characterization of substrates nature of the inorganic substrate may dis- qualify a particular display technology. b For instance, since a centrifugation step is Biopanning necessary during the biopanning process (Figure 2b) when one is working with Binding powder substrates, phage display is suitable for finding peptides that bind to pow- Washing cycles to disrupt ders,5–9 but the CSD system is not. weak interactions Centrifuging a bacterial cell with flagella with the substrate would shear off the flagella and the attached peptides from the cell. Binding Elution of bound phages the cells to the powder would not be pos- or cells from surfaces sible.9,67 Similarly, while both phage and cell-surface display are normally suitable for panning on single crystals, tightly Repeat biopanning bound cells or phages may be difficult to several rounds for recover once they are bound to a material. enrichment of tight binders Thus, it may not be possible to determine the sequences of their high-affinity peptides. In such cases, the use of the CSD sys- Replication of phage tem may be advantageous since all binders or growing of cells have an equal likelihood of being recov- ered following flagellar breakage. Another Extraction of DNA important factor affecting the efficiency of HWTR DPGI KT the display system, and consequently the LIGK TSLI GGP selection of the strong binders, is monitor- Obtaining inorganic binding amino-acid sequences ing of the stability of the inorganic solid under the selection conditions.9 Many materials rapidly develop an oxide layer Figure 2. A schematic of the combinatorial mutagenesis, namely phage and cell-surface on their surfaces, expose different crystal- display, in selecting short amino-acid sequences with affinity for solid inorganic materials (from Reference 55). lographic faces to the solvent, and may become chemically or physically modified when incubated in the biological media quantitatively the degree of peptide speci- essential step in the design and assembly used during the panning process. ficity for a given solid as compared to non- of functional inorganic structures. specific interactions with other solids of Although protein–surface interactions Solid Binding and Recognition by similar chemical compositions or surface have been the object of considerable Peptides and Assembly structures (e.g., binding to aragonitic ver- research,72 the fundamental basis of how Biocombinatorial techniques provide sus calcitic CaCO3, to gold versus plat- peptides recognize inorganics remains simple knowledge about a peptide’s affin- inum or silver, or to silica versus alumina largely unknown.42,43,70–77 The specificity of a ity for an inorganic surface; however, or titania).68,69 Ideally, the knowledge of peptide for a surface may originate from more complete information about the the molecular structure and amino-acid both chemical (e.g., H-bonding, polarity, mechanism(s) or the strength of binding sequence of a GEPI and the basis of the stereochemistry, and charge effects) and and assembly of a genetically selected peptide’s recognition of the solid will physical (crystallography, topology, size, peptide to a solid will be necessary for the allow for further tailoring and manipula- and morphology) recognition mecha- robust use of peptides in practical application of its functional properties.70,71 nisms.78,79 Understanding the compositions.55,68 Also, it is essential to evaluate Acquiring this knowledge, therefore, is an tional, sequence, and structural features

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instrumental in binding could eventually result in tailoring the function, recognition, Binding, Structure, Molecular Recognition, & Assembly or assembly characteristics of peptides either alone or as a part of designer proteins. Designer proteins include DNA binding a Kinetics of b c Molecular d Structure Assembly proteins, light-emitting/harvesting proteins, Binding Recognition self-assembling proteins, and viral cap- 12–15,55 Nonspecific Binding SPR CD MolecularMolecular IImprintmprint sid. Chimera (peptide-protein hybrid 3 10 AFM 5 0 ) x 10

constructions) of surface-specific peptide -1 -5 -10 dmol binders connected to designer proteins 2 -15 HABP-1 Nonspecific Specific Binding -20 HABP-2 could act as multifunctional linkers having -25 assembly

(deg cm 185 195 205 215 225 235 245 255 M SPR Shift (nm) unique physical functionalities such as solid θ Wavelength (nm) binding proteins with enzymatic function. Time (mins) HABP1 & HABP2 3rGBP1 on Gr(0001) Toward the overarching goal of creating GEPI – Binding to Solids Molecular Polypod multifunctional molecular tools through N NMR AFM hybrid GEPI-protein structures, computa- Solid A Specific, tional biology and materials tools—such Supramolecular as molecular dynamics70,80 and bioinfor- self-assembly matics81 that draw on experimental Solid B C Frequency Difference (HZ) parameters70,82—are useful instruments to Time (secs) 3rGBP1 PPtBPtBP onon PPt(110)t(110) 3rGBP1 on Au(111) accelerate the process of understanding the molecular recognition of solids by GEPI. These methods are essential for the Figure 3. The four established steps for molecular characterization of a genetically implementation of chimera in engineering engineered polypeptide for inorganics (GEPI) as a viable technological molecular tool. or medical applications. In the absence of (a) The kinetics of solid binding and specificity of inorganic-binding peptides for a given 83 complete understanding about the nature solid could be determined by surface-plasmon-resonance (SPR) spectroscopy. At the of peptide binding, a well-established pro- same time, whether a GEPI is specific for a solid surface compared to another solid is determined by quartz-crystal microbalance as well as SPR.68 (b) Spectroscopy, such tocol that involves four basic steps as circular dichroism70 and nuclear magnetic resonance,70 could provide molecular (described in Figure 3) characterizes the architecture. HABP1 and HABP2 are two hydroxyapatite binding peptides. 3rGBP1 is a binding kinetics, molecular architecture, gold binding peptide. (c) In the absence of structural details, computational modeling such and surface structure of a GEPI on an inor- as molecular dynamics could provide molecular conformation and shed light on the ganic material. The first step evaluates the mechanism of crystallographic surface recognition.71 Finally, (d) supramolecular self- kinetics of molecular binding involving an assembly of the peptide on the crystallographic surface of the inorganic material could be assessment of the specificity of the peptide visualized by atomic force microscopy as demonstrated here for a gold-binding peptide on 55 toward various surfaces55,68,83 using modi- graphite(0001) and Au(111). fied surface plasmon resonance (SPR) spectroscopy.84 It is often coupled with GEPI as Molecular Synthesizers, overcome utilizing the unique opportuni- quartz-crystal microbalance (QCM)85 Erectors, and Assemblers in ties offered by the biomimetic approach at (Figure 3a).55,68,83 Significant progress has Nanotechnology and Medicine the molecular scale. The approaches used been made using both SPR55,68 and Three key issues in using peptides to to genetically select and characterize QCM.55,83 However, both of these tech- make functional nanomaterials are the GEPIs are discussed in Figures 2 and 3. niques—especially the latter—have limi- synthesis of the individual material com- Some of the utility is outlined in Figure 4 tations for the study of very small ponents, controlled linking of multicom- and also is demonstrated in other articles molecules.86 Once a strong binder is iden- ponent systems, and multidimensional in this issue. tified, its detailed molecular architecture is assembly.55 To make any multicomponent Controlled binding and assembly of characterized by various spectroscopy material system (“multimaterial”) practi- proteins onto inorganic substrates is at the techniques—most notably with circular cally useful—in addition to the intrinsic core of bionanotechnology and biological dichorism (CD) and nuclear-magnetic- magnetic, photonic, or electronic proper- materials engineering.55,76,91,92 GEPI pro- resonance (NMR) spectroscopy (Figure ties that are derived from nanometer vides the molecular means to anchor, cou- 3b).70,82,86 The third step involves computa- dimensions89,90—each component may ple, brace, display, and assemble functional tional modeling to understand possible need to be chemically modified so as to molecules, nanoparticles, and structures.1 peptide recognition of crystallography of assemble the system controllably and effi- The examples in Figure 4 provide a sum- the solid surface and is especially useful in ciently.17–20 As is well-recognized in mary of potential utilizations of GEPI. the absence of experimental data.70,79,80 nanoscience, numerous challenges must Once peptides with short amino-acid Finally, knowledge of surface coverage, be addressed before nanotechnology can sequences (7–15 amino acids) are geneti- assembly, and supramolecular architec- be fully implemented successfully into cally selected, sorted, and categorized, tural formation55 is necessary for rational working devices.89,90 The challenges their molecular properties—including utility of GEPI for specific applications. include synthesizing nanostructures (e.g., structures and binding functions—are Atomic force microscopy (AFM) gives particles, rods, and tubes) with uniform characterized (Figures 2 and 3). These quantitative molecular-level and nanos- size and shape; controlling their composi- include post-selection engineering in tructure imaging (Figure 3d).55 The use of tion, bulk structure, and surface character- which multiple repeats of linear or cyclic AFM imaging here is similar to the evalu- istics; and organizing them in one, two, architectures for the select sequences are ation of thiol-based self-assembled mono- and three dimensions with predictable designed and synthesized.55,68,83 The next layers (SAM), ubiquitous among the spatial distribution. If biology is to be a step represents a “molecular tool box,” synthetic molecular linkers.87,88 guide, some of these challenges could be which is an inorganic-binding peptide

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Targeted as quantum dots—at specific regions of Enzymes multimaterial micropatterned surfaces Directed Cytocompatibility (for example, an Au and Pt pattern on sil- Assembly PDMS stamp w/o GEPI Cell-Signaling Assays ica). This is a step toward assembly of nanophotonic entities.93 Another example Au substrate SV F PDL OC CM Patterning of SH-(CH ) -(OC H ) -OH Pt 2 11 2 4 3 Day 811 14 21 6912 involves using GEPIs as molecular erec-

0 tors. Linking the GEPIs to enzymes with Au SiO 1 µm the genes of a virus or bacterium allows x BMP-2 10 w/ GEPI (ng/ml) for directed self-assembly at specific Au substrate 50 94 Pt Self-assembly of AP-5GBP regions of solid substrates. In bionan- 100 otechnology, growth and proliferation Au of various cell types on solid surfaces Au substrate 1 µm as arrays are possible through the cell- 20 µm Activity assay of AP-5GBP signaling characteristics of the hydroxyapatite (HA) binding peptides.95 It may be Bionanotechnology 50 µm possible to regenerate some hard tissues such as enamel and cementum49,50 using Regenerative GEPIs and their derivatives to direct (i) Medicine Enamel nucleation, growth rate, and morphogenesis of HA nanoparticles. One example is the regulation of calcium-phosphate formation using HA binding peptides as 5 µm synthesizers in biomaterialization.95 (ii) Nanotechnology applications include GEPI: using GEPIs such as AgBP (Ag-binding peptide) or QBP (quartz binding peptide) Molecular Cementum Toolbox as part of a fusion protein assembled on a specific material. These materials include metal (e.g., Ag) nanoparticles94 or silicon 1 µm nanowires96 for target recognition via localized surface-plasmon- resonance spec- w/o GEPI w/ GEPI troscopy97 or electronic ring detectors,98 respectively. These platforms, once opti- mized, could be the basis of new highly (iii) sensitive biosensors. (See the article by 200 nm Chen et al. in this issue regarding the util- Target Biomaterialization ity of DNA or peptides for these purposes.) Nanotechnology Probe Prospects Ag or Au The utilization of GEPIs as building i Nanoparticles bio–GEPI blocks and molecular tools in designing, Nanowire Plasmonics synthesizing, and assembling materials

bare bio–GEPI systems necessitates the combination of + new concepts from the fields of biology, Enzyme Electronic medicine, computation, informatics, mate-

Ring Detectors Normalized Scattering rials science, condensed-matter physics, 250 nm 55 Wavelength (nm) chemistry, and engineering. Molecular tailoring of specific peptide− solid interactions could have a significant impact in Figure 4. Genetically identified and molecularly characterized genetically engineered areas in which inorganic materials offer peptides for inorganics (GEPIs) could form a molecular toolbox for a wide range of several novel, immediate practical advan- applications from materialization to medicine and nanotechnology. Selected GEPIs from the toolbox could be chosen as building blocks for their specific ability to synthesize, erect, and tages. The attachment of biomolecules in assemble. (i), (ii), and (iii) represent GEPIs as a nanoparticle immobilizer, a genetic fusing particular proteins onto solid supports is agent, and a bifunctional system, respectively. A bifunctional system could couple two fundamental in the development of nanoparticles, or a nanoparticle and a functional molecule, simultaneously. The images advanced biosensors for detection of are sampled experimental results where GEPIs are used in diverse applications: in bio- pathogens, drug screening,91 biosepara- nanotechnology to immobilize quantum dots and targeted immobilize enzymes, in tions systems, and diagnostics in medi- regenerative medicine for surface functionalization within cytocompatibility assays and cine98 such as those used in cancer hard-tissue regeneration through materialization using peptides as nucleators and growth therapeutics.92 Protein adsorption and modifiers, and in nanotechnology as molecular erectors to immobilize probe molecules in macromolecular interactions at solid sur- electronic ring detectors and localized surface-enhanced plasmonics. faces play key roles in the performance of implants and in regenerative medi- data bank:1,9,55 a collection of fully charac- tical applications, at the final step, include cine.76,99 (See the article by Rughani et al. in terized select GEPIs ready to be utilized the utility of GEPI as universal ink in the this issue.) Proteins and DNA adsorbed for a wide range of applications. The prac- targeted assembly of nanoparticles—such specifically onto solid substrates are used

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Rieke, Ed., 74. D.J.H. Gaskin, K. Strack, E.N. Vulfson, 9. M. Sarikaya, C. Tamerler, D.T. Schwartz, 174, 109 (MRS, Pittsburgh, PA, 1990). Biotechnol. Lett. 22, 1211 (2000). F. Baneyx, Annu. Rev. Mater. Res. 34, 373 (2004). 41. M. Sarikaya, I.A. Aksay, in Results and 75. J.N. Cha, K. Shimizu, Y. Zhou, S.C. 10. K.I. Sano, H. Sasaki, K. Shiba, Langmuir 21, Problems in Cell Differentiation, S.T. Case, Ed., 19, Christiansen, B.F. Chmelka, G.D. Stucky, D.E. 3090 (2005). 1 (Springer, New York, 1992). Morse, Proc. Nat. Acad. Sci. U.S.A. 96, 361 (1999). 11. H. Dai, W.-S. Choe, C. K. Thai, M.Sarikaya, 42. S. Mann, Nature 332, 119 (1988). 76. B. Ratner, F. Schoen, A. Hoffman, J. Lemons, B.A. Traxler, F. Baneyx, D.T. Schwartz, J. Am. 43. S. Weiner, L. Addadi, J. Mater. Chem. 7, 689 Biomaterials Science: Introduction to Materials in Ceram. Soc. 127, 15637 (2005). (1997). Medicine (Academic Press, San Diego, 1996). 12. R.A. McMillan, J. Howard, N.J. Zaluzec, 44. I.A. Aksay, E. Baer, M. Sarikaya, T. Tirrell, 77. M. Mrksich, Curr. Opin. Chem. Biol. 6, 794 H.K. Kagawa, R. Mogul, Y.F. Li, C.D. Paavola, Eds., MRS Proc. 255 (MRS, Pittsburgh, PA, 1994). (2002). J.D. Trent, J. Am. Chem. Soc. 127, 2800 (2005). 45. B.L.M. Hogan, Genes Dev. 10 (13), 1580 (1996). 78. L. Pauling, Nature 24 (10), 1375 (1946).

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79. J.V. Barth, J. Weckesser, G. Trimarchi, M. Methods and Phenomena (Elsevier, New York, 94. T. Kacar, C. So, C. Tamerler, M. Sarikaya, Vladimirova, A. De Vita, C. Cai, H. Brune, P. 1984). J. MSE-C (2008) in press. Gunter, K. Kern, J. Am. Chem. Soc. 124, 7991 (2002). 86. L.E. Bailey, D. Kambhampati, K.K. 95. M. Gungormus, H. Fong, I.W. Kim, J.S. 80. S.D. Tomasio, T.R. Walsh, Mol. Phys. 105, Kanazawa, W. Knoll, C.W. Frank, Langmuir 18, Evans, C. Tamerler, M. Sarikaya, Biomacromole- 221 (2007). 479 (2002). cules (2008) in press. 81. J.S. Evans, Curr. Opin. Colloid Interface Sci. 8, 87. G.M. Whitesides, J.P. Mathias, C.T. Seto, 96. B.A. Parviz, Trends in Microbiol. 14 (9), 373 48 (2003). Science 254, 1312 (1991). (2006). 82. E.E. Oren, C. Tamerler, D. Sahin, M. 88. R. Schreiber, Prog. Surf. Sci. 65, 151 (2000). 97. Y.N. Xia, N.J. Halas, MRS Bull. 30, 338 Hnilova, U.O.S. Seker, M. Sarikaya, R. 89. M.L. Roukes, Understanding Nanotechnology (2005). Samudrala, Bioinformatics 23, 2816 (2007). (Warner Books, New York, 2002). 98. P.N. Prasad, Biomaterials and Nanophotonics 83. O.U.S. Seker, B. Wilson, S. Dincer, I.W. Kim, 90. M. Ratner, D. Ratner, Nanotechnology (Wiley, Hoboken, NJ, 2004). E.E. Oren, J.S. Evans, C. Tamerler, M. Sarikaya, (Prentice Hall, Upper Saddle River, NJ, 2003). 99. J.D. Hartgerink, E. Beniash, S.I. Stupp, Langmuir 23, 7895 (2007). 91. P. Cutler, Proteomics 3, 3 (2003). Science 294, 1684 (2001). 84. L.S. Jung, C.T. Campbell, T.M. Chinowsky, 92. S. Zhang, Nat. Biotechnol. 21, 1171 (2003). 100. M.F. Temlin, D. Stoll, M. Schrenk, Trends M.N. Mar, S.S. Yee, Langmuir 14, 5636 (1988). 93. C. Tamerler, M. Duman, E.E. Oren, Biotechnol. 20, 160 (2002). ■ 85. A.W. Czenderna, C. Lu, Applications of M. Gungormus X. Xiong, T. Kacar, B.A. Parviz, Piezoelectric Quartz Crystal Microbalances, M. Sarikaya, Small 2, 1372 (2006).

Candan Tamerler Mehmet Sarikaya Yeechi Chen David S. Ginger Keiko Munechika

Candan Tamerler, Guest tides, their utilization in director of the Genetically scanning-probe tech- high honors at Dartmouth Editor for this issue biofabrication, engineer- Engineered Materials niques) to molecular College. Chen’s research of MRS Bulletin, is a ing signing biocompatible Science and Engineering biomimetics—where investigates the optical professor and chair in surfaces, and developing Center—a National genetically engineered properties of fluorophores the Molecular Biology novel detection and prob- Science Foundation peptides are used as near metal nanoparticles and Genetics ing systems—all relevant Materials Research building blocks for tai- and the exploration of Department, and also in bionanotechnology, Science and Engineering lored materials structures bio-inspired methods of director of the nanomedicine, and Center—at the University for predictive functions. self-assembly. Molecular Biology- nanotechnology. Tamerler of Washington. Sarikaya Sarikaya can be Chen can be reached Biotechnology and has published more than received his PhD degree reached at the Genetically at the University of Genetics Research Center 60 articles and four book (1982) at the University of Engineered Materials Washington, Department at Istanbul Technical chapters, and has California at Berkeley. Science and Engineering of Physics, PO Box University. Tamerler presented more than 50 Afterward, Sarikaya Center, Department of 351560, Seattle, WA holds a long-term visiting invited and keynote joined the faculty at the Materials Science and 98195-1560, USA; professor position in lectures. University of Engineering, Roberts Hall, e-mail yeechi@u. materials science and Tamerler can be reached Washington. In addition, PO Box 352120, washington.edu. engineering at the at Department of he has been a visiting University of Washington, University of Molecular Biology and professor at Princeton Seattle, WA 98195-2120, John Spencer Evans is a Washington. Her research Genetics, Istanbul University, Nagoya USA; tel. 206-543-0724; fax professor of chemistry interests range from Technical University, University, and Istanbul 206-543-6381; e-mail and biochemistry at New expression and purifica- Istanbul, Turkey; tel. +90- Technical University. [email protected]. York University and tion of biological mole- 212-2862251; fax +90-212- Over the years, his edu. works in the area of cules to protein-based 2862253; e-mail tamerler@ research has evolved protein-mediated materials and systems itu.edu.tr or candan@ from structure- Yeechi Chen is a PhD biomineralization and where the peptide func- u.washington.edu. property correlations degree candidate study- genetically engineered tionalities are genetically in metals, ceramics, ing physics under the peptides. Evans received controlled. In molecular Mehmet Sarikaya, Guest high-temperature advisement of David his PhD degree in chem- biomimetics, Tamerler’s Editor for this issue of superconductors and Ginger at the University istry from the California research interests cover MRS Bulletin, is a profes- semiconductors, and of Washington. She Institute of Technology. the genetic selection of sor of materials science nano systems (via earned her AB degree The major focus of his material- specific pep- and engineering, and electron-optical and (2000) in physics with research is the contribu-

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Rajesh R. Naik Ersin Emre Oren Ronak V. Rughani Ram Samudrala Ken-Ichi Sano

tions of polypeptide physics with Neil and investigating the Genetically Engineered β-hairpins to modulate structure to the functional Greenham in the opto- optical properties of fluo- Materials Science and mechanical properties of aspects of biomineraliza- electronics group at the rophores placed near Engineering Center at the hydrogels for tissue- tion and nanotechnology University of Cambridge metal nanoparticles utiliz- University of Washington engineering and drug- proteins using nuclear (UK). Ginger was a joint ing biological assembly. (UW), working with pro- delivery applications. magnetic resonance National Institutes of Munechika can be fessors Ram Samudrala Rughani can be sprectroscopy and other Health and DuPont reached at the University and Mehmet Sarikaya. reached at 024 Lammot biophysical techniques. postdoctoral fellow at of Washington, Prior to his appointment du Pont Laboratory, Evans is considered the Northwestern University Department of Chemistry, at UW, Oren earned his Department of world expert in this area. in Chad Mirkin’s labora- PO Box 351700, Seattle, PhD degree in metallurgi- Chemistry and His current funding tory. His current research WA 98195-1700, USA; cal and materials engi- Biochemistry, University spans the National centers on the physical e-mail keikoc@ u. neering at Middle East of Delaware, Newark, Institutes of Health (NIH), chemistry of nanostruc- washington.edu. Technical University in DE 19716, USA; tel. 302- the National Science tured materials with Ankara, Turkey. Oren’s 831-0624; e-mail Foundation (NSF), and applications in optoelec- Rajesh R. Naik is the research focuses on com- [email protected]. the U.S. Department of tronics and sensing. In technical adviser in the putational materials sci- Energy. Evans’ awards addition, Ginger is a Nanostructured and ence in bio-nanomaterials, Ram Samudrala is an include Young Research Corporation Biological Materials bio-interfaces, and com- associate professor in the Investigator Awards from Cottrell Scholar, an Alfred Branch and group leader putational design of Department of the Whitaker Foundation P. Sloan Foundation at the Materials and inorganic-binding Microbiology at UW. and the Office of Army Research Fellow, a Manufacturing (RX) peptides. Using computational Research, and a CAREER Camille Dreyfus Teacher- Directorate, Air Force Oren can be reached at approaches, his research award from the National Scholar, and a winner of Research Laboratory the Department of is directed at under- Science Foundation. the Presidential Early (AFRL), at Wright- Materials Science and standing protein folding, Evans can be reached Career Award for Patterson Air Force Engineering, PO Box structure, function, and at the Laboratory for Scientists and Engineers. Base, Ohio. He received 352120, University of evolution—at the single- Chemical Physics, Ginger can be reached his PhD degree (1998) Washington, Seattle, WA molecule level as well as New York University, at the University of in biological sciences 98195–2120, USA; tel. the genomic, proteomic, 345 E. 24th St., New Washington, Department from Carnegie 206-616-6643; fax 206-543- and organismal levels. York, NY 10010, USA; tel. of Chemistry, PO Box Mellon University. 3100; e-mail eeoren@ Samudrala’s work has 212-998-9605; fax 212- 351700, Seattle, WA Naik has authored u.washington.edu. led to more than 70 pub- 995-4087; e-mail 98195-1700, USA; tel. 206- more than 85 peer- lications and freely [email protected]. 685-2331; fax 206-685- reviewed articles and Ronak V. Rughani has reproducible software for 8665; e-mail ginger@ received the Air Force been a graduate student molecular and systems David S. Ginger is an chem.washington.edu; Scientist Award in 2007. with professor Joel P. modeling. His research is assistant professor of Web site http://faculty. Naik can be reached at Schneider in the funded by the NIH, the chemistry and an adjunct washington.edu/dginger. the Materials and Department of Chemistry NSF, the Gates assistant professor of Manufacturing and Biochemistry at the Foundation, and the UW physics at the University Keiko Munechika is a Directorate, Air Force University of Delaware Advanced Technology of Washington. He PhD degree candidate Research Laboratory, since 2003. Rughani Initiative in Infectious earned dual BS degrees studying chemistry at the AFRL/RXBP Bldg. 654, received his BS degree Diseases. Samudrala’s (1997) in chemistry and University of Washington 2941 Hobson Way, (1998) in pharmaceutical honors include the NSF physics at Indiana under the guidance of Wright-Patterson Air sciences from the CAREER award (2005). University. Ginger then David Ginger. She earned Force Base, OH 45433- University of Bombay Also, he was named one received a British her BS degree (2003) in 7750, USA; tel. 937-255- and his MS degree (2003) of the world’s top young Marshall Scholarship and chemistry at Evergreen 9717; e-mail rajesh.naik@ in organic chemistry innovators (TR100) by a National Science State College. wpafbaf.mil. from the University of MIT Technology Review Foundation graduate fel- Munechika’s research Louisiana at Monroe. His (2003), he was the UW lowship. He completed interests focus on synthe- Ersin Emre Oren is a research focuses on New Investigator Science his PhD degree (2001) in sizing metal nanoparticles research associate in the designing self-assembling in Medicine Lecturer

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Joel P. Schneider Kiyotaka Shiba Joseph M. Slocik Morley O. Stone Melanie M. Tomczak

(2004), and he is a Searle Fellow in the School Biochemistry at the at Wright-Patterson Air Scholar. of Medicine at the University of Tokyo. Force Base, Ohio. Stone Samudrala can be University of He was then a postdoc- received his PhD degree reached at the Pennsylvania. He began toral research fellow at in biochemistry from Department of Micro- his independent career at the Massachusetts Carnegie Mellon biology, PO Box 357242 UD in 1999. Schneider’s Institute of Technology University. He currently University of Washington, research group is inter- until joining the Cancer leads the cellular dynam- Seattle, WA 98195-7242, ested in developing bio- Institute in 1991. Shiba’s ics and engineering group USA; tel. 206-732-6122, logical materials for use in research interests include at RH. Stone also has fax 206-732-6055; e-mail therapeutic-delivery and the evolution of genes, authored more than 70 ram@compbio. tissue-regenerative thera- protein engineering, and peer-reviewed publica- washington.edu. pies. His honors include bio-nanotechnology. tions and four technical the DuPont Young Shiba can be reached book chapters, serves on Tiffany R. Walsh Ken-Ichi Sano is a post- Investigator Award and at the Department of the editorial board of two doctoral fellow in the the University of Protein Engineering, international scientific Department of Protein Delaware’s Francis Alison Cancer Institute, Koto, journals, and is a fellow of chemistry and holds a Engineering at the Young Professor Award. Tokyo 135-8550, Japan; AFRL and the joint position in the Cancer Institute, Japanese In addition, Schneider e-mail kshiba@ jfcr.or.jp. International Optical Chemistry Department Foundation for Cancer serves as an associate edi- Engineering Society. and the Centre for Research. He received his tor for Peptide Science. Joseph M. Slocik is a Scientific Computing at BS degree from Osaka Schneider can be research scientist in the Melanie M. Tomczak is the University of City University and his reached at 009 Lammot Nanostructured and a research scientist in the Warwick (UK). She PhD degree from the du Pont Laboratory, Biological Materials Nanostructured and earned her PhD degree in Nagoya University. Department of Branch, Materials and Biological Materials theoretical chemistry at Sano’s research interests Chemistry and Manufacturing Branch, Materials and the University of include the interface Biochemistry, University Directorate, Air Force Manufacturing Cambridge and then held between biomolecules of Delaware, Newark, Research Laboratory, at Directorate, AFRL, at a Glasstone Fellowship in and inorganic materials, DE 19716, USA; tel. 302- Wright-Patterson Air Wright-Patterson Air the Department of self-organization at 831-3024; e-mail Force Base, Ohio. He Force Base, Ohio. She Materials at the interfaces, and biominer- [email protected]. received his BS degree received her BS degree University of Oxford. alization. (1997) in forensic chem- from the University of Walsh is active in the Sano can be reached Kiyotaka Shiba is mem- istry from Ohio Illinois and her PhD area of biomolecule- by e-mail at kenichi. ber and chief of the University and his PhD degree from the inorganic simulation and sano@ jfcr.or.jp. Department of Protein degree (2004) in chem- University of California is a member of the Engineering at the istry from Vanderbilt at Davis, working in Engineering and Joel P. Schneider is an Cancer Institute, University—under the John Crowe’s laboratory. Physical Sciences associate professor of Japanese Foundation for advisement of professor Tomczak was a postdoc- Research Council-funded Chemistry and Cancer Research, in David Wright. Slocik’s toral fellow with Peter Materials Modeling Biochemistry at the Tokyo. Shiba received his projects currently involve Davies at Queen’s Consortium, “Modeling University of Delaware BS and PhD degrees in biomimetic synthesis, University in Canada the Biological Interface (UD). Schneider received molecular biology from bio-derived catalysts, before obtaining her cur- with Materials.” his BS degree in chemistry the Faculty of Science at and peptide-mediated rent position at AFRL. Walsh can be reached from the University of Kyoto University, where assembly. Her projects include bio- at the Department Akron, and his PhD he studied the mecha- mimetic synthesis and of Chemistry, University degree in chemistry from nism of protein secretion Morley O. Stone is the biofunctionalization of of Warwick, Coventry, Texas A&M University. using bacterial genetics. Senior Scientist (ST) of inorganic nanoparticles. CV4 7AL, UK; tel. After receiving his Afterward, Shiba worked Molecular Systems +44-24-765-74448; degrees, Schneider as an assistant professor Biotechnology at the Tiffany R. Walsh is an fax +44-24-764-24112; became a George W. in the Department of Human Effectiveness associate professor in e-mail t_walsh@ Raiziss Postdoctoral Biophysics and (RH) Directorate, AFRL, theoretical/computational warwick.ac.uk. ■

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